These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
196 related articles for article (PubMed ID: 8396660)
1. Two regions of the herpes simplex virus type 1 UL42 protein are required for its functional interaction with the viral DNA polymerase. Monahan SJ; Barlam TF; Crumpacker CS; Parris DS J Virol; 1993 Oct; 67(10):5922-31. PubMed ID: 8396660 [TBL] [Abstract][Full Text] [Related]
2. Deletions of the carboxy terminus of herpes simplex virus type 1 UL42 define a conserved amino-terminal functional domain. Tenney DJ; Hurlburt WW; Bifano M; Stevens JT; Micheletti PA; Hamatake RK; Cordingley MG J Virol; 1993 Apr; 67(4):1959-66. PubMed ID: 8383221 [TBL] [Abstract][Full Text] [Related]
3. Mutations in the C terminus of herpes simplex virus type 1 DNA polymerase can affect binding and stimulation by its accessory protein UL42 without affecting basal polymerase activity. Tenney DJ; Micheletti PA; Stevens JT; Hamatake RK; Matthews JT; Sanchez AR; Hurlburt WW; Bifano M; Cordingley MG J Virol; 1993 Jan; 67(1):543-7. PubMed ID: 8380091 [TBL] [Abstract][Full Text] [Related]
4. Analysis of in vitro activities of herpes simplex virus type 1 UL42 mutant proteins: correlation with in vivo function. Thornton KE; Chaudhuri M; Monahan SJ; Grinstead LA; Parris DS Virology; 2000 Sep; 275(2):373-90. PubMed ID: 10998337 [TBL] [Abstract][Full Text] [Related]
6. Role of the carboxy terminus of herpes simplex virus type 1 DNA polymerase in its interaction with UL42. Marsden HS; Murphy M; McVey GL; MacEachran KA; Owsianka AM; Stow ND J Gen Virol; 1994 Nov; 75 ( Pt 11)():3127-35. PubMed ID: 7964622 [TBL] [Abstract][Full Text] [Related]
7. The essential in vivo function of the herpes simplex virus UL42 protein correlates with its ability to stimulate the viral DNA polymerase in vitro. Reddig PJ; Grinstead LA; Monahan SJ; Johnson PA; Parris DS Virology; 1994 May; 200(2):447-56. PubMed ID: 8178434 [TBL] [Abstract][Full Text] [Related]
8. Interaction of herpes simplex virus type 1 DNA polymerase and the UL42 accessory protein with a model primer template. Gottlieb J; Challberg MD J Virol; 1994 Aug; 68(8):4937-45. PubMed ID: 8035492 [TBL] [Abstract][Full Text] [Related]
9. Mutations that specifically impair the DNA binding activity of the herpes simplex virus protein UL42. Chow CS; Coen DM J Virol; 1995 Nov; 69(11):6965-71. PubMed ID: 7474115 [TBL] [Abstract][Full Text] [Related]
10. The herpes simplex virus type 1 DNA polymerase accessory protein, UL42, contains a functional protease-resistant domain. Hamatake RK; Bifano M; Tenney DJ; Hurlburt WW; Cordingley MG J Gen Virol; 1993 Oct; 74 ( Pt 10)():2181-9. PubMed ID: 8409941 [TBL] [Abstract][Full Text] [Related]
11. The extreme C terminus of herpes simplex virus DNA polymerase is crucial for functional interaction with processivity factor UL42 and for viral replication. Digard P; Bebrin WR; Weisshart K; Coen DM J Virol; 1993 Jan; 67(1):398-406. PubMed ID: 8380085 [TBL] [Abstract][Full Text] [Related]
12. The C-terminal third of UL42, a HSV-1 DNA replication protein, is dispensable for viral growth. Gao M; DiTusa SF; Cordingley MG Virology; 1993 Jun; 194(2):647-53. PubMed ID: 8389077 [TBL] [Abstract][Full Text] [Related]
13. Identification of crucial hydrogen-bonding residues for the interaction of herpes simplex virus DNA polymerase subunits via peptide display, mutational, and calorimetric approaches. Bridges KG; Chow CS; Coen DM J Virol; 2001 Jun; 75(11):4990-8. PubMed ID: 11333878 [TBL] [Abstract][Full Text] [Related]
14. Sequences at the C-terminus of the herpes simplex virus type 1 UL30 protein are dispensable for DNA polymerase activity but not for viral origin-dependent DNA replication. Stow ND Nucleic Acids Res; 1993 Jan; 21(1):87-92. PubMed ID: 8382792 [TBL] [Abstract][Full Text] [Related]
15. The catalytic subunit of herpes simplex virus type 1 DNA polymerase contains a nuclear localization signal in the UL42-binding region. Loregian A; Piaia E; Cancellotti E; Papini E; Marsden HS; Palù G Virology; 2000 Jul; 273(1):139-48. PubMed ID: 10891416 [TBL] [Abstract][Full Text] [Related]
16. The herpes simplex virus type 1 UL42 gene product: a subunit of DNA polymerase that functions to increase processivity. Gottlieb J; Marcy AI; Coen DM; Challberg MD J Virol; 1990 Dec; 64(12):5976-87. PubMed ID: 2173776 [TBL] [Abstract][Full Text] [Related]
17. Mutations that increase DNA binding by the processivity factor of herpes simplex virus affect virus production and DNA replication fidelity. Jiang C; Komazin-Meredith G; Tian W; Coen DM; Hwang CB J Virol; 2009 Aug; 83(15):7573-80. PubMed ID: 19474109 [TBL] [Abstract][Full Text] [Related]
18. The essential 65-kilodalton DNA-binding protein of herpes simplex virus stimulates the virus-encoded DNA polymerase. Gallo ML; Dorsky DI; Crumpacker CS; Parris DS J Virol; 1989 Dec; 63(12):5023-9. PubMed ID: 2555539 [TBL] [Abstract][Full Text] [Related]
19. Functional interaction between the herpes simplex-1 DNA polymerase and UL42 protein. Hernandez TR; Lehman IR J Biol Chem; 1990 Jul; 265(19):11227-32. PubMed ID: 2193033 [TBL] [Abstract][Full Text] [Related]
20. Evidence against a simple tethering model for enhancement of herpes simplex virus DNA polymerase processivity by accessory protein UL42. Chaudhuri M; Parris DS J Virol; 2002 Oct; 76(20):10270-81. PubMed ID: 12239303 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]